Secretion of recombinant xylanase in Lactococcus lactis using signal peptides Usp45 and Spk1

Roslan AM 1 , Mustafa Kamil A 2 , Chandran C 2 , Song AA 3 , Yusoff K 2 , Abdul Rahim R 1

Affiliations 

  • 1 Department of Cell and Molecular Biology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400, Serdang, Selangor, Malaysia
  • 2 Department of Microbiology, Faculty of Biotechnology & Biomolecular Sciences, Universiti Putra Malaysia, 43400, Serdang, Selangor, Malaysia
  • 3 Department of Microbiology, Faculty of Biotechnology & Biomolecular Sciences, Universiti Putra Malaysia, 43400, Serdang, Selangor, Malaysia. adelene@upm.edu.my
Biotechnol Lett, 2020 Sep;42(9):1727-1733.
PMID: 32335791 DOI: 10.1007/s10529-020-02894-1

Abstract

OBJECTIVE: The effect of two signal peptides, namely Usp45 and Spk1 on the secretion of xylanase in Lactococcus lactis was analysed.

RESULTS: Xylanase was successfully expressed in Lactococcus lactis. Recombinant xylanase fused to either signal peptide Usp45 or Spk1 showed halo zone on Remazol Brilliant Blue-Xylan plates. This indicated that the xylanase was successfully secreted from the cell. The culture supernatants of strains secreting the xylanase with help of the Spk1 and Usp45 signal peptides contained 49.7 U/ml and 34.4 U/ml of xylanase activity, respectively.

CONCLUSION: Although Usp45 is the most commonly used signal peptide when secreting heterologous proteins in Lactococcus lactis, this study shows that Spk1 isolated from Pediococcus pentosaceus was superior to Usp45 in regard to xylanase protein secretion.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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